{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Enzymes designated “LIPM” have been characterized in a variety of biological contexts, highlighting their diverse roles in lipid‐processing and sugar activation. In one bacterial system, the cloned "}, {"type": "b", "children": [{"type": "t", "text": "lipM"}]}, {"type": "t", "text": " gene from "}, {"type": "i", "children": [{"type": "t", "text": "Pseudomonas moraviensis"}]}, {"type": "t", "text": " encodes an extracellular lipase that is remarkably eurythermic and thermostable. This enzyme exhibits a broad temperature range (10–95 °C), is modulated by specific metal ions, and efficiently hydrolyzes substrates—including algal oil—to significantly enrich polyunsaturated fatty acids, thereby representing an attractive biocatalyst for industrial processes (1)."}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In a different context, a distinct enzyme also designated LipM has been identified as a key component in the biosynthetic pathway of peptidyl nucleoside antibiotics. Here, LipM functions as a UTP:5‑amino‑5‑deoxy‑α‑D‑ribose‑1‑phosphate uridylyltransferase that generates an activated nucleotide sugar donor. This reaction is a critical step in the unique ribosylation cascade that installs an unusual aminoribosyl moiety—a modification essential for the bioactivity of these antibiotics (2).\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n Additionally, bioinformatic analyses of mammalian acid lipases have classified LIPM as one of the epidermal lipases, suggesting a specialized role in skin tissues. Although its precise biochemical activities in epidermal homeostasis require further investigation, LIPM in this context is thought to participate in lipid hydrolysis and remodeling processes that contribute to barrier formation and function (3).\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n Together, these studies illustrate that “LIPM” refers to functionally distinct enzymes whose activities range from lipid hydrolysis in robust, industrially relevant bacterial systems, to nucleotide‐sugar activation in complex secondary metabolite biosynthesis, and to specialized lipid processing in mammalian epidermal tissues.\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n (1)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "(2)"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "(3)."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wenjuan Yang, Hai Cao, Li Xu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A novel eurythermic and thermostale lipase LipM from Pseudomonas moraviensis M9 and its application in the partial hydrolysis of algal oil."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Biotechnol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12896-015-0214-0"}], "href": "https://doi.org/10.1186/s12896-015-0214-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26463643"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26463643"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Xiuling Chi, Pallab Pahari, Koichi Nonaka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Biosynthetic origin and mechanism of formation of the aminoribosyl moiety of peptidyl nucleoside antibiotics."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Am Chem Soc (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/ja206304k"}], "href": "https://doi.org/10.1021/ja206304k"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21819104"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21819104"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Roger S Holmes, Laura A Cox, John L VandeBerg "}, {"type": "b", "children": [{"type": "t", "text": "Comparative studies of mammalian acid lipases: Evidence for a new gene family in mouse and rat (Lipo)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Comp Biochem Physiol Part D Genomics Proteomics (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cbd.2010.05.004"}], "href": "https://doi.org/10.1016/j.cbd.2010.05.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20598663"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20598663"}]}]}]}